Journal
CELL CHEMICAL BIOLOGY
Volume 25, Issue 7, Pages 840-+Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2018.03.011
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Funding
- Wellcome Trust [109854/Z/15/Z]
- Biotechnology and Biological Sciences Research Council [BB/K017292/1]
- Stavros S. Niarchos Foundation for Charity grant
- Imperial College London Institute of Chemical Biology EPSRC CDT studentship award
- BBSRC [1622063, BB/K017292/1] Funding Source: UKRI
- Wellcome Trust [109854/Z/15/Z] Funding Source: Wellcome Trust
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The role ofmembrane lipids in modulating eukaryotic transporter assembly and function remains unclear. We investigated the effect of membrane lipids in the structure and transport activity of the purine transporter UapA from Aspergillus nidulans. We found that UapA exists mainly as a dimer and that two lipid molecules bind per UapA dimer. We identified three phospholipid classes that co-purified with UapA: phosphatidylcholine, phosphatidylethanolamine (PE), and phosphatidylinositol (PI). UapA delipidation caused dissociation of the dimer into monomers. Subsequent addition of PI or PE rescued the UapA dimer and allowed recovery of bound lipids, suggesting a central role of these lipids in stabilizing the dimer. Molecular dynamics simulations predicted a lipid binding site near the UapA dimer interface. Mutational analyses established that lipid binding at this site is essential for formation of functional UapA dimers. We propose that structural lipids have a central role in the formation of functional, dimeric UapA.
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